Cadherins are homophilic adhesion molecules at cell–cell junctions that mediate crosstalk between adhesion complexes and the actin cytoskeleton through interaction with intracellular binding partners such as catenins. Microtubules are an important component of the cellular cytoskeleton, but their role in cadherin-mediated adhesions remains unclear. Therefore, René-Marc Mège and colleagues (p. 1660) set out to analyse and compare MT recruitment and dynamics in the context of N-cadherin- and integrin-mediated adhesions on surfaces that are coated with either recombinant N-cadherin or fibronectin (FN). They find that, compared with integrin-based focal adhesions, N-cadherin engagement limits MT elongation and the targeting of their plus ends towards cadherin adhesions. In addition, MTs are also excluded from the areas in lamellopodia where cadherin adhesions form. As the authors show here, engagement of N-cadherin triggers a fast retrograde actin flow and the stabilisation of an actomyosin belt at the rear of this adhesion zone. Using pharmacological means of actin perturbation, they demonstrate that this belt is the main obstacle to MT plus-end penetration within the adhesion zone. The authors then use substrates composed of stripes alternating of N-cadherin and FN coating to eliminate possible effects of cell shape, and confirm that engagement of either integrin or N-cadherin has opposite effects on the MT network. Interestingly, MTs that invade the adhesion areas may destabilise N-cadherin-based adhesions, pointing to crosstalk between cadherin adhesion, MTs and the actin network. This functional network, the authors suggest, may be instrumental in establishing the front–rear polarity of adherent cells.